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| | ==NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase== | | ==NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase== |
| - | <StructureSection load='2khk' size='340' side='right'caption='[[2khk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2khk' size='340' side='right'caption='[[2khk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2khk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KHK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2khk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHK FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2khk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khk OCA], [http://pdbe.org/2khk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2khk RCSB], [http://www.ebi.ac.uk/pdbsum/2khk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2khk ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2khk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khk OCA], [https://pdbe.org/2khk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khk RCSB], [https://www.ebi.ac.uk/pdbsum/2khk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATPF_ECOLI ATPF_ECOLI]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).<ref>PMID:1682301</ref> Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).<ref>PMID:1682301</ref> | + | [https://www.uniprot.org/uniprot/ATPF_ECOLI ATPF_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).<ref>PMID:1682301</ref> Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).<ref>PMID:1682301</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Biukovic, G]] | + | [[Category: Biukovic G]] |
| - | [[Category: Gayen, S]] | + | [[Category: Gayen S]] |
| - | [[Category: Gruber, G]] | + | [[Category: Gruber G]] |
| - | [[Category: Priya, R]] | + | [[Category: Priya R]] |
| - | [[Category: Vivekanandan, S]] | + | [[Category: Vivekanandan S]] |
| - | [[Category: Atp synthesis]]
| + | |
| - | [[Category: B30-82]]
| + | |
| - | [[Category: Cell inner membrane]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: F1fo atp synthase]]
| + | |
| - | [[Category: Hydrogen ion transport]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Nmr spectroscopy]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
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| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ATPF_ECOLI F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).[1] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Subunit b, the peripheral stalk of bacterial F(1)F(o) ATP synthases, is composed of a membrane-spanning and a soluble part. The soluble part is divided into tether, dimerization, and delta-binding domains. The first solution structure of b30-82, including the tether region and part of the dimerization domain, has been solved by nuclear magnetic resonance, revealing an alpha-helix between residues 39 and 72. In the solution structure, b30-82 has a length of 48.07 A. The surface charge distribution of b30-82 shows one side with a hydrophobic surface pattern, formed by alanine residues. Alanine residues 61, 68, 70, and 72 were replaced by single cysteines in the soluble part of subunit b, b22-156. The cysteines at positions 61, 68, and 72 showed disulfide formation. In contrast, no cross-link could be formed for the A70C mutant. The patterns of disulfide bonding, together with the circular dichroism spectroscopy data, are indicative of an adjacent arrangement of residues 61, 68, and 72 in both alpha-helices in b22-156.
Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase.,Priya R, Biukovic G, Gayen S, Vivekanandan S, Gruber G J Bacteriol. 2009 Dec;191(24):7538-44. Epub 2009 Oct 9. PMID:19820091[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McCormick KA, Cain BD. Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. PMID:1682301
- ↑ McCormick KA, Cain BD. Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. PMID:1682301
- ↑ Priya R, Biukovic G, Gayen S, Vivekanandan S, Gruber G. Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase. J Bacteriol. 2009 Dec;191(24):7538-44. Epub 2009 Oct 9. PMID:19820091 doi:10.1128/JB.00540-09
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